A0A0Q9WDS4 · A0A0Q9WDS4_DROVI

Function

function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site27ATP (UniProtKB | ChEBI)
Binding site90-91ATP (UniProtKB | ChEBI)
Binding site120-123ATP (UniProtKB | ChEBI)
Binding site121Mg2+ (UniProtKB | ChEBI); catalytic
Binding site166-168substrate; ligand shared between dimeric partners; in other chain
Active site168Proton acceptor
Binding site203substrate; ligand shared between dimeric partners
Binding site210-212substrate; ligand shared between dimeric partners; in other chain
Binding site266substrate; ligand shared between dimeric partners; in other chain
Binding site294substrate; ligand shared between dimeric partners
Binding site300-303substrate; ligand shared between dimeric partners; in other chain
Binding site480beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site537-541beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site575beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site582-584beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site638beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site664beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners
Binding site670-673beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain
Binding site745beta-D-fructose 2,6-bisphosphate (UniProtKB | ChEBI); allosteric activator; ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Component6-phosphofructokinase complex
Molecular Function6-phosphofructokinase activity
Molecular FunctionAMP binding
Molecular FunctionATP binding
Molecular Functionfructose-6-phosphate binding
Molecular Functionidentical protein binding
Molecular Functionmetal ion binding
Molecular Functionmonosaccharide binding
Biological Processcanonical glycolysis
Biological Processfructose 1,6-bisphosphate metabolic process
Biological Processfructose 6-phosphate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent 6-phosphofructokinase
  • EC number
  • Short names
    ATP-PFK
    ; Phosphofructokinase
  • Alternative names
    • Phosphohexokinase

Gene names

    • Name
      Dvir\GJ22388
    • ORF names
      Dvir_GJ22388

Organism names

  • Taxonomic identifier
  • Strain
    • Tucson 15010-1051.87
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila

Accessions

  • Primary accession
    A0A0Q9WDS4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-392N-terminal catalytic PFK domain 1
Domain20-324Phosphofructokinase
Domain411-696Phosphofructokinase
Region411-788C-terminal regulatory PFK domain 2

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    788
  • Mass (Da)
    86,781
  • Last updated
    2016-01-20 v1
  • Checksum
    31B67A7472AF341C
MNSDINQRFLARGSQRDKGLAVFTSGGDSQGMNAAVRACVRMAIYLGCKVYFIREGYQGMVDGGECIQEASWASVSSIIHRGGTIIGSARCQDFRERAGRLKAANNLIQRGITNLVVIGGDGSLTGANLFRQEWSSLLDELSKNGTITSEQKEKYNVLHIVGLVGSIDNDFCGTDMTIGTDTALHRIIEAIDAISSTAYSHQRTFIMEVMGRHCGYLALVAGLSSEADFIFIPEMPPKTDWPDRLCFQLAQERKAGQRLNIVIVAEGAMDREGNPITAEDVRKVIDERLKHDARITVLGHVQRGGNPSAFDRILACRMGAEATLALMEATEESVPVVISLDGNQTVRVPLMECVERTQAVAKAMKERRWADAVKLRGRSFERNLETYKMLTRLKPPKECFDEQGKGIEGFRLAVMHIGAPACGMNAAVRSFVRNAIYRGDVVYGINDGVEGLIAGNVRVLGWSDVSGWVGQGGAYLGTKRTLPEGKFKEIAARLKEFKIQGLLIIGGFESYHAAGQISDQRDNYPEFCIPIVVVPATISNNVPGTEFSLGCDTGLNEITEICDRIRQSAQGTKRRVFVIETMGGYCGYLATLAGLAGGADAAYIYEEKFSIKDLQQDVYHMASKMAEGVSRGLILRNEKASENYTTDFIYRLYSEEGKGLFTCRMNILGHMQQGGSPTPFDRNMGTKMAAKCVDWLATQIKNNIDANGVVNCKSTDTATLLGIVARQYRFSPLVDLIGETNFDQRIPKKQWWLRLRPLLRILAKHDSAYEEEGMYITVEEECATDAVA

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0Q9W5R3A0A0Q9W5R3_DROVIDvir\GJ223881029
A0A0Q9W5X8A0A0Q9W5X8_DROVIDvir\GJ223881029
A0A0Q9W693A0A0Q9W693_DROVIDvir\GJ223881029
B4LMG6B4LMG6_DROVIDvir\GJ22388788

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CH940648
EMBL· GenBank· DDBJ
KRF80423.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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